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Database: PDB
Entry: 1OX6
LinkDB: 1OX6
Original site: 1OX6 
HEADER    TRANSFERASE, LYASE                      01-APR-03   1OX6              
TITLE     TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX CYCLIZATION        
TITLE    2 REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE HISHF;               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: AMIDOTRANSFERASE AND CYCLASE DOMAINS;                      
COMPND   5 SYNONYM: HISTIDINE BIOSYNTHESIS BIFUNCTIONAL AMIDOTRANSFERASE; IGP   
COMPND   6 SYNTHASE; IMGP SYNTHASE; IGPS; GLUTAMINE AMIDOTRANSFERASE:CYCLASE;   
COMPND   7 EC: 2.4.2.-, 4.1.3.-;                                                
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: HIS7;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    COMPLEX CYCLIZATION; IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE,             
KEYWDS   2 TRANSFERASE, LYASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.N.CHAUDHURI,J.L.SMITH                                               
REVDAT   3   16-AUG-23 1OX6    1       REMARK SEQADV LINK                       
REVDAT   2   24-FEB-09 1OX6    1       VERSN                                    
REVDAT   1   17-JUN-03 1OX6    0                                                
JRNL        AUTH   B.N.CHAUDHURI,S.C.LANGE,R.S.MYERS,V.J.DAVISSON,J.L.SMITH     
JRNL        TITL   TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX           
JRNL        TITL 2 CYCLIZATION REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE 
JRNL        TITL 3 SYNTHASE: CRYSTAL STRUCTURES OF A TERNARY COMPLEX AND THE    
JRNL        TITL 4 FREE ENZYME                                                  
JRNL        REF    BIOCHEMISTRY                  V.  42  7003 2003              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12795595                                                     
JRNL        DOI    10.1021/BI034320H                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.S.MYERS,J.R.JENSEN,I.L.DERAS,J.L.SMITH,V.J.DAVISSON        
REMARK   1  TITL   SUBSTRATE-INDUCED CHANGES IN THE AMMONIA CHANNEL FOR         
REMARK   1  TITL 2 IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE                        
REMARK   1  REF    BIOCHEMISTRY                  V.  42  7013 2003              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI034314L                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1517144.100                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 44.7000                        
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 46100                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2317                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7240                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 373                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.017                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8256                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 281                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.00000                                              
REMARK   3    B22 (A**2) : -9.66000                                             
REMARK   3    B33 (A**2) : 0.66000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.32                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.28                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.350                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.870                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.340 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.240 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.930 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.930 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 29.29                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DISORDERED REGIONS WERE MODELED           
REMARK   3  STEREOCHEMICALLY                                                    
REMARK   4                                                                      
REMARK   4 1OX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000018763.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03320                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-2                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47205                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : 0.10600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 1JVN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PEG MME 5000, MES,     
REMARK 280  PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       48.50000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.40000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.40000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       48.50000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A   257                                                      
REMARK 465     LYS A   258                                                      
REMARK 465     GLY A   259                                                      
REMARK 465     ASP A   260                                                      
REMARK 465     GLN A   261                                                      
REMARK 465     TYR A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     VAL A   264                                                      
REMARK 465     ARG A   265                                                      
REMARK 465     GLU A   266                                                      
REMARK 465     LYS A   267                                                      
REMARK 465     SER A   268                                                      
REMARK 465     ASP A   269                                                      
REMARK 465     GLY A   270                                                      
REMARK 465     LYS A   271                                                      
REMARK 465     GLY A   272                                                      
REMARK 465     VAL A   273                                                      
REMARK 465     ARG A   274                                                      
REMARK 465     ASN A   275                                                      
REMARK 465     SER A   301                                                      
REMARK 465     PHE A   302                                                      
REMARK 465     ARG A   303                                                      
REMARK 465     GLU A   551                                                      
REMARK 465     GLU A   552                                                      
REMARK 465     THR B   257                                                      
REMARK 465     LYS B   258                                                      
REMARK 465     GLY B   259                                                      
REMARK 465     ASP B   260                                                      
REMARK 465     GLN B   261                                                      
REMARK 465     TYR B   262                                                      
REMARK 465     ASP B   263                                                      
REMARK 465     VAL B   264                                                      
REMARK 465     ARG B   265                                                      
REMARK 465     GLU B   266                                                      
REMARK 465     LYS B   267                                                      
REMARK 465     SER B   268                                                      
REMARK 465     ASP B   269                                                      
REMARK 465     GLY B   270                                                      
REMARK 465     LYS B   271                                                      
REMARK 465     GLY B   272                                                      
REMARK 465     VAL B   273                                                      
REMARK 465     ARG B   274                                                      
REMARK 465     ASN B   275                                                      
REMARK 465     SER B   301                                                      
REMARK 465     PHE B   302                                                      
REMARK 465     ARG B   303                                                      
REMARK 465     GLU B   551                                                      
REMARK 465     GLU B   552                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  -2        7.05   -165.59                                   
REMARK 500    CYS A  83     -110.44     55.44                                   
REMARK 500    PRO A  97      -37.90    -37.35                                   
REMARK 500    ASP A 106       32.07    -75.57                                   
REMARK 500    ASN A 185     -118.19     49.00                                   
REMARK 500    PRO A 217      154.49    -48.83                                   
REMARK 500    TYR A 234        7.23     58.96                                   
REMARK 500    ILE A 299       67.69   -114.26                                   
REMARK 500    PHE A 324       53.30    -98.57                                   
REMARK 500    GLN A 413      -19.27    -49.96                                   
REMARK 500    SER A 500      117.89     83.80                                   
REMARK 500    ALA A 523      -92.32   -123.83                                   
REMARK 500    SER B  -2       11.97   -174.60                                   
REMARK 500    CYS B  83     -111.83     58.17                                   
REMARK 500    PRO B  97      -37.10    -37.97                                   
REMARK 500    ASN B 185     -117.18     50.06                                   
REMARK 500    PRO B 217      154.01    -47.20                                   
REMARK 500    TYR B 234        8.94     57.84                                   
REMARK 500    ASN B 249     -165.54    -79.07                                   
REMARK 500    ILE B 299       67.53   -115.68                                   
REMARK 500    PHE B 324       52.60    -98.66                                   
REMARK 500    SER B 500      118.22     81.85                                   
REMARK 500    ALA B 523      -93.29   -124.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A 902  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A  -3   N                                                      
REMARK 620 2 SER A  -2   N    75.4                                              
REMARK 620 3 HIS A  -1   ND1 106.3 176.3                                        
REMARK 620 4 HIS A  -1   N   153.5  78.3 100.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 901  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B  -3   N                                                      
REMARK 620 2 SER B  -2   N    79.5                                              
REMARK 620 3 HIS B  -1   ND1 101.3 172.6                                        
REMARK 620 4 HIS B  -1   N   161.2  81.9  97.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE POP B 999                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JVN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1OX4   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1OX5   RELATED DB: PDB                                   
DBREF  1OX6 A    1   552  UNP    P33734   HIS5_YEAST       1    552             
DBREF  1OX6 B    1   552  UNP    P33734   HIS5_YEAST       1    552             
SEQADV 1OX6 GLY A   -3  UNP  P33734              CLONING ARTIFACT               
SEQADV 1OX6 SER A   -2  UNP  P33734              CLONING ARTIFACT               
SEQADV 1OX6 HIS A   -1  UNP  P33734              CLONING ARTIFACT               
SEQADV 1OX6 GLY B   -3  UNP  P33734              CLONING ARTIFACT               
SEQADV 1OX6 SER B   -2  UNP  P33734              CLONING ARTIFACT               
SEQADV 1OX6 HIS B   -1  UNP  P33734              CLONING ARTIFACT               
SEQRES   1 A  555  GLY SER HIS MET PRO VAL VAL HIS VAL ILE ASP VAL GLU          
SEQRES   2 A  555  SER GLY ASN LEU GLN SER LEU THR ASN ALA ILE GLU HIS          
SEQRES   3 A  555  LEU GLY TYR GLU VAL GLN LEU VAL LYS SER PRO LYS ASP          
SEQRES   4 A  555  PHE ASN ILE SER GLY THR SER ARG LEU ILE LEU PRO GLY          
SEQRES   5 A  555  VAL GLY ASN TYR GLY HIS PHE VAL ASP ASN LEU PHE ASN          
SEQRES   6 A  555  ARG GLY PHE GLU LYS PRO ILE ARG GLU TYR ILE GLU SER          
SEQRES   7 A  555  GLY LYS PRO ILE MET GLY ILE CYS VAL GLY LEU GLN ALA          
SEQRES   8 A  555  LEU PHE ALA GLY SER VAL GLU SER PRO LYS SER THR GLY          
SEQRES   9 A  555  LEU ASN TYR ILE ASP PHE LYS LEU SER ARG PHE ASP ASP          
SEQRES  10 A  555  SER GLU LYS PRO VAL PRO GLU ILE GLY TRP ASN SER CYS          
SEQRES  11 A  555  ILE PRO SER GLU ASN LEU PHE PHE GLY LEU ASP PRO TYR          
SEQRES  12 A  555  LYS ARG TYR TYR PHE VAL HIS SER PHE ALA ALA ILE LEU          
SEQRES  13 A  555  ASN SER GLU LYS LYS LYS ASN LEU GLU ASN ASP GLY TRP          
SEQRES  14 A  555  LYS ILE ALA LYS ALA LYS TYR GLY SER GLU GLU PHE ILE          
SEQRES  15 A  555  ALA ALA VAL ASN LYS ASN ASN ILE PHE ALA THR GLN PHE          
SEQRES  16 A  555  HIS PRO GLU LYS SER GLY LYS ALA GLY LEU ASN VAL ILE          
SEQRES  17 A  555  GLU ASN PHE LEU LYS GLN GLN SER PRO PRO ILE PRO ASN          
SEQRES  18 A  555  TYR SER ALA GLU GLU LYS GLU LEU LEU MET ASN ASP TYR          
SEQRES  19 A  555  SER ASN TYR GLY LEU THR ARG ARG ILE ILE ALA CYS LEU          
SEQRES  20 A  555  ASP VAL ARG THR ASN ASP GLN GLY ASP LEU VAL VAL THR          
SEQRES  21 A  555  LYS GLY ASP GLN TYR ASP VAL ARG GLU LYS SER ASP GLY          
SEQRES  22 A  555  LYS GLY VAL ARG ASN LEU GLY LYS PRO VAL GLN LEU ALA          
SEQRES  23 A  555  GLN LYS TYR TYR GLN GLN GLY ALA ASP GLU VAL THR PHE          
SEQRES  24 A  555  LEU ASN ILE THR SER PHE ARG ASP CYS PRO LEU LYS ASP          
SEQRES  25 A  555  THR PRO MET LEU GLU VAL LEU LYS GLN ALA ALA LYS THR          
SEQRES  26 A  555  VAL PHE VAL PRO LEU THR VAL GLY GLY GLY ILE LYS ASP          
SEQRES  27 A  555  ILE VAL ASP VAL ASP GLY THR LYS ILE PRO ALA LEU GLU          
SEQRES  28 A  555  VAL ALA SER LEU TYR PHE ARG SER GLY ALA ASP LYS VAL          
SEQRES  29 A  555  SER ILE GLY THR ASP ALA VAL TYR ALA ALA GLU LYS TYR          
SEQRES  30 A  555  TYR GLU LEU GLY ASN ARG GLY ASP GLY THR SER PRO ILE          
SEQRES  31 A  555  GLU THR ILE SER LYS ALA TYR GLY ALA GLN ALA VAL VAL          
SEQRES  32 A  555  ILE SER VAL ASP PRO LYS ARG VAL TYR VAL ASN SER GLN          
SEQRES  33 A  555  ALA ASP THR LYS ASN LYS VAL PHE GLU THR GLU TYR PRO          
SEQRES  34 A  555  GLY PRO ASN GLY GLU LYS TYR CYS TRP TYR GLN CYS THR          
SEQRES  35 A  555  ILE LYS GLY GLY ARG GLU SER ARG ASP LEU GLY VAL TRP          
SEQRES  36 A  555  GLU LEU THR ARG ALA CYS GLU ALA LEU GLY ALA GLY GLU          
SEQRES  37 A  555  ILE LEU LEU ASN CYS ILE ASP LYS ASP GLY SER ASN SER          
SEQRES  38 A  555  GLY TYR ASP LEU GLU LEU ILE GLU HIS VAL LYS ASP ALA          
SEQRES  39 A  555  VAL LYS ILE PRO VAL ILE ALA SER SER GLY ALA GLY VAL          
SEQRES  40 A  555  PRO GLU HIS PHE GLU GLU ALA PHE LEU LYS THR ARG ALA          
SEQRES  41 A  555  ASP ALA CYS LEU GLY ALA GLY MET PHE HIS ARG GLY GLU          
SEQRES  42 A  555  PHE THR VAL ASN ASP VAL LYS GLU TYR LEU LEU GLU HIS          
SEQRES  43 A  555  GLY LEU LYS VAL ARG MET ASP GLU GLU                          
SEQRES   1 B  555  GLY SER HIS MET PRO VAL VAL HIS VAL ILE ASP VAL GLU          
SEQRES   2 B  555  SER GLY ASN LEU GLN SER LEU THR ASN ALA ILE GLU HIS          
SEQRES   3 B  555  LEU GLY TYR GLU VAL GLN LEU VAL LYS SER PRO LYS ASP          
SEQRES   4 B  555  PHE ASN ILE SER GLY THR SER ARG LEU ILE LEU PRO GLY          
SEQRES   5 B  555  VAL GLY ASN TYR GLY HIS PHE VAL ASP ASN LEU PHE ASN          
SEQRES   6 B  555  ARG GLY PHE GLU LYS PRO ILE ARG GLU TYR ILE GLU SER          
SEQRES   7 B  555  GLY LYS PRO ILE MET GLY ILE CYS VAL GLY LEU GLN ALA          
SEQRES   8 B  555  LEU PHE ALA GLY SER VAL GLU SER PRO LYS SER THR GLY          
SEQRES   9 B  555  LEU ASN TYR ILE ASP PHE LYS LEU SER ARG PHE ASP ASP          
SEQRES  10 B  555  SER GLU LYS PRO VAL PRO GLU ILE GLY TRP ASN SER CYS          
SEQRES  11 B  555  ILE PRO SER GLU ASN LEU PHE PHE GLY LEU ASP PRO TYR          
SEQRES  12 B  555  LYS ARG TYR TYR PHE VAL HIS SER PHE ALA ALA ILE LEU          
SEQRES  13 B  555  ASN SER GLU LYS LYS LYS ASN LEU GLU ASN ASP GLY TRP          
SEQRES  14 B  555  LYS ILE ALA LYS ALA LYS TYR GLY SER GLU GLU PHE ILE          
SEQRES  15 B  555  ALA ALA VAL ASN LYS ASN ASN ILE PHE ALA THR GLN PHE          
SEQRES  16 B  555  HIS PRO GLU LYS SER GLY LYS ALA GLY LEU ASN VAL ILE          
SEQRES  17 B  555  GLU ASN PHE LEU LYS GLN GLN SER PRO PRO ILE PRO ASN          
SEQRES  18 B  555  TYR SER ALA GLU GLU LYS GLU LEU LEU MET ASN ASP TYR          
SEQRES  19 B  555  SER ASN TYR GLY LEU THR ARG ARG ILE ILE ALA CYS LEU          
SEQRES  20 B  555  ASP VAL ARG THR ASN ASP GLN GLY ASP LEU VAL VAL THR          
SEQRES  21 B  555  LYS GLY ASP GLN TYR ASP VAL ARG GLU LYS SER ASP GLY          
SEQRES  22 B  555  LYS GLY VAL ARG ASN LEU GLY LYS PRO VAL GLN LEU ALA          
SEQRES  23 B  555  GLN LYS TYR TYR GLN GLN GLY ALA ASP GLU VAL THR PHE          
SEQRES  24 B  555  LEU ASN ILE THR SER PHE ARG ASP CYS PRO LEU LYS ASP          
SEQRES  25 B  555  THR PRO MET LEU GLU VAL LEU LYS GLN ALA ALA LYS THR          
SEQRES  26 B  555  VAL PHE VAL PRO LEU THR VAL GLY GLY GLY ILE LYS ASP          
SEQRES  27 B  555  ILE VAL ASP VAL ASP GLY THR LYS ILE PRO ALA LEU GLU          
SEQRES  28 B  555  VAL ALA SER LEU TYR PHE ARG SER GLY ALA ASP LYS VAL          
SEQRES  29 B  555  SER ILE GLY THR ASP ALA VAL TYR ALA ALA GLU LYS TYR          
SEQRES  30 B  555  TYR GLU LEU GLY ASN ARG GLY ASP GLY THR SER PRO ILE          
SEQRES  31 B  555  GLU THR ILE SER LYS ALA TYR GLY ALA GLN ALA VAL VAL          
SEQRES  32 B  555  ILE SER VAL ASP PRO LYS ARG VAL TYR VAL ASN SER GLN          
SEQRES  33 B  555  ALA ASP THR LYS ASN LYS VAL PHE GLU THR GLU TYR PRO          
SEQRES  34 B  555  GLY PRO ASN GLY GLU LYS TYR CYS TRP TYR GLN CYS THR          
SEQRES  35 B  555  ILE LYS GLY GLY ARG GLU SER ARG ASP LEU GLY VAL TRP          
SEQRES  36 B  555  GLU LEU THR ARG ALA CYS GLU ALA LEU GLY ALA GLY GLU          
SEQRES  37 B  555  ILE LEU LEU ASN CYS ILE ASP LYS ASP GLY SER ASN SER          
SEQRES  38 B  555  GLY TYR ASP LEU GLU LEU ILE GLU HIS VAL LYS ASP ALA          
SEQRES  39 B  555  VAL LYS ILE PRO VAL ILE ALA SER SER GLY ALA GLY VAL          
SEQRES  40 B  555  PRO GLU HIS PHE GLU GLU ALA PHE LEU LYS THR ARG ALA          
SEQRES  41 B  555  ASP ALA CYS LEU GLY ALA GLY MET PHE HIS ARG GLY GLU          
SEQRES  42 B  555  PHE THR VAL ASN ASP VAL LYS GLU TYR LEU LEU GLU HIS          
SEQRES  43 B  555  GLY LEU LYS VAL ARG MET ASP GLU GLU                          
HET     NI  A 902       1                                                       
HET    SO4  A 801       5                                                       
HET    SO4  A 802       5                                                       
HET    SO4  A 806       5                                                       
HET     NI  B 901       1                                                       
HET    SO4  B 803       5                                                       
HET    SO4  B 804       5                                                       
HET    POP  B 999       9                                                       
HETNAM      NI NICKEL (II) ION                                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM     POP PYROPHOSPHATE 2-                                                 
FORMUL   3   NI    2(NI 2+)                                                     
FORMUL   4  SO4    5(O4 S 2-)                                                   
FORMUL  10  POP    H2 O7 P2 2-                                                  
FORMUL  11  HOH   *281(H2 O)                                                    
HELIX    1   1 GLN A   15  HIS A   23  1                                   9    
HELIX    2   2 PRO A   34  ASP A   36  5                                   3    
HELIX    3   3 ILE A   39  GLY A   41  5                                   3    
HELIX    4   4 TYR A   53  ASN A   62  1                                  10    
HELIX    5   5 PHE A   65  SER A   75  1                                  11    
HELIX    6   6 CYS A   83  LEU A   89  5                                   7    
HELIX    7   7 VAL A   94  SER A   96  5                                   3    
HELIX    8   8 SER A  155  ASN A  163  1                                   9    
HELIX    9   9 PRO A  194  LYS A  196  5                                   3    
HELIX   10  10 GLY A  198  LYS A  210  1                                  13    
HELIX   11  11 ALA A  221  LEU A  227  1                                   7    
HELIX   12  12 SER A  232  GLY A  235  5                                   4    
HELIX   13  13 GLY A  277  GLN A  288  1                                  12    
HELIX   14  14 LEU A  307  ASP A  309  5                                   3    
HELIX   15  15 PRO A  311  LYS A  321  1                                  11    
HELIX   16  16 ALA A  346  SER A  356  1                                  11    
HELIX   17  17 THR A  365  GLU A  376  1                                  12    
HELIX   18  18 PRO A  386  TYR A  394  1                                   9    
HELIX   19  19 ALA A  396  ALA A  398  5                                   3    
HELIX   20  20 GLN A  413  ASP A  415  5                                   3    
HELIX   21  21 VAL A  451  LEU A  461  1                                  11    
HELIX   22  22 LEU A  482  ALA A  491  1                                  10    
HELIX   23  23 PRO A  505  LYS A  514  1                                  10    
HELIX   24  24 GLY A  524  HIS A  527  1                                   4    
HELIX   25  25 VAL A  533  HIS A  543  1                                  11    
HELIX   26  26 GLN B   15  HIS B   23  1                                   9    
HELIX   27  27 PRO B   34  ASP B   36  5                                   3    
HELIX   28  28 ILE B   39  GLY B   41  5                                   3    
HELIX   29  29 TYR B   53  ASN B   62  1                                  10    
HELIX   30  30 PHE B   65  SER B   75  1                                  11    
HELIX   31  31 CYS B   83  LEU B   89  5                                   7    
HELIX   32  32 VAL B   94  SER B   96  5                                   3    
HELIX   33  33 SER B  155  ASN B  163  1                                   9    
HELIX   34  34 PRO B  194  LYS B  196  5                                   3    
HELIX   35  35 GLY B  198  LEU B  209  1                                  12    
HELIX   36  36 ALA B  221  LEU B  227  1                                   7    
HELIX   37  37 SER B  232  GLY B  235  5                                   4    
HELIX   38  38 GLY B  277  GLN B  288  1                                  12    
HELIX   39  39 LEU B  307  ASP B  309  5                                   3    
HELIX   40  40 PRO B  311  LYS B  321  1                                  11    
HELIX   41  41 ALA B  346  SER B  356  1                                  11    
HELIX   42  42 THR B  365  GLU B  376  1                                  12    
HELIX   43  43 PRO B  386  TYR B  394  1                                   9    
HELIX   44  44 ALA B  396  ALA B  398  5                                   3    
HELIX   45  45 GLN B  413  ASP B  415  5                                   3    
HELIX   46  46 VAL B  451  LEU B  461  1                                  11    
HELIX   47  47 LEU B  482  ALA B  491  1                                  10    
HELIX   48  48 PRO B  505  LYS B  514  1                                  10    
HELIX   49  49 GLY B  524  HIS B  527  1                                   4    
HELIX   50  50 VAL B  533  HIS B  543  1                                  11    
SHEET    1   A 7 GLU A  27  VAL A  31  0                                        
SHEET    2   A 7 VAL A   3  ILE A   7  1  N  VAL A   4   O  GLU A  27           
SHEET    3   A 7 LEU A  45  GLY A  49  1  N  ILE A  46   O  HIS A   5           
SHEET    4   A 7 ILE A  79  CYS A  83  1  N  MET A  80   O  LEU A  45           
SHEET    5   A 7 ILE A 187  THR A 190  1  N  PHE A 188   O  ILE A  79           
SHEET    6   A 7 GLU A 176  LYS A 184 -1  N  LYS A 184   O  ILE A 187           
SHEET    7   A 7 LYS A 167  TYR A 173 -1  N  TYR A 173   O  GLU A 176           
SHEET    1   B 2 GLU A 121  ASN A 125  0                                        
SHEET    2   B 2 TYR A 143  HIS A 147 -1  N  HIS A 147   O  GLU A 121           
SHEET    1   C 8 ALA A 519  GLY A 522  0                                        
SHEET    2   C 8 ARG A 239  ARG A 247  1  N  ARG A 239   O  CYS A 520           
SHEET    3   C 8 GLU A 293  ILE A 299  1  N  GLU A 293   O  ALA A 242           
SHEET    4   C 8 PRO A 326  GLY A 330  1  N  PRO A 326   O  VAL A 294           
SHEET    5   C 8 LYS A 360  ILE A 363  1  N  LYS A 360   O  VAL A 329           
SHEET    6   C 8 VAL A 399  PRO A 405  1  N  VAL A 400   O  VAL A 361           
SHEET    7   C 8 GLU A 465  CYS A 470  1  N  GLU A 465   O  ILE A 401           
SHEET    8   C 8 PRO A 495  ALA A 498  1  N  PRO A 495   O  ILE A 466           
SHEET    1   D 2 PRO A 405  VAL A 410  0                                        
SHEET    2   D 2 TYR A 433  CYS A 438 -1  N  GLN A 437   O  LYS A 406           
SHEET    1   E 7 VAL B  28  VAL B  31  0                                        
SHEET    2   E 7 VAL B   4  ILE B   7  1  N  VAL B   4   O  GLN B  29           
SHEET    3   E 7 LEU B  45  GLY B  49  1  N  ILE B  46   O  HIS B   5           
SHEET    4   E 7 ILE B  79  CYS B  83  1  N  MET B  80   O  LEU B  45           
SHEET    5   E 7 ILE B 187  THR B 190  1  N  PHE B 188   O  ILE B  79           
SHEET    6   E 7 GLU B 176  LYS B 184 -1  N  LYS B 184   O  ILE B 187           
SHEET    7   E 7 LYS B 167  TYR B 173 -1  N  TYR B 173   O  GLU B 176           
SHEET    1   F 2 GLU B 121  ASN B 125  0                                        
SHEET    2   F 2 TYR B 143  HIS B 147 -1  N  HIS B 147   O  GLU B 121           
SHEET    1   G 8 CYS B 520  GLY B 522  0                                        
SHEET    2   G 8 ILE B 240  VAL B 246  1  N  ILE B 241   O  CYS B 520           
SHEET    3   G 8 GLU B 293  ASN B 298  1  N  GLU B 293   O  ALA B 242           
SHEET    4   G 8 PRO B 326  GLY B 330  1  N  PRO B 326   O  VAL B 294           
SHEET    5   G 8 LYS B 360  ILE B 363  1  N  LYS B 360   O  VAL B 329           
SHEET    6   G 8 VAL B 399  PRO B 405  1  N  VAL B 400   O  VAL B 361           
SHEET    7   G 8 GLU B 465  CYS B 470  1  N  GLU B 465   O  ILE B 401           
SHEET    8   G 8 PRO B 495  ALA B 498  1  N  PRO B 495   O  ILE B 466           
SHEET    1   H 2 PRO B 405  VAL B 410  0                                        
SHEET    2   H 2 TYR B 433  CYS B 438 -1  N  GLN B 437   O  LYS B 406           
LINK         N   GLY A  -3                NI    NI A 902     1555   1555  2.33  
LINK         N   SER A  -2                NI    NI A 902     1555   1555  2.15  
LINK         ND1 HIS A  -1                NI    NI A 902     1555   1555  1.95  
LINK         N   HIS A  -1                NI    NI A 902     1555   1555  2.00  
LINK         N   GLY B  -3                NI    NI B 901     1555   1555  2.23  
LINK         N   SER B  -2                NI    NI B 901     1555   1555  1.98  
LINK         ND1 HIS B  -1                NI    NI B 901     1555   1555  2.23  
LINK         N   HIS B  -1                NI    NI B 901     1555   1555  2.02  
CISPEP   1 VAL A  119    PRO A  120          0         0.73                     
CISPEP   2 VAL B  119    PRO B  120          0         0.63                     
SITE     1 AC1  4 GLY B  -3  SER B  -2  HIS B  -1  MET B   1                    
SITE     1 AC2  5 HIS A  -1  GLY A  -3  SER A  -2  MET A   1                    
SITE     2 AC2  5 TYR B 425                                                     
SITE     1 AC3  2 GLY A 364  THR A 365                                          
SITE     1 AC4  5 GLY A 475  SER A 500  GLY A 501  HOH A 961                    
SITE     2 AC4  5 HOH A1034                                                     
SITE     1 AC5  3 LYS B 158  LYS B 170  LYS B 343                               
SITE     1 AC6  5 GLY B 331  GLY B 364  THR B 365  HOH B1107                    
SITE     2 AC6  5 HOH B1126                                                     
SITE     1 AC7  4 SER A 130  ASN A 132  HOH A1027  LYS B 493                    
SITE     1 AC8 11 ASP B 474  GLY B 475  ASN B 477  SER B 500                    
SITE     2 AC8 11 GLY B 501  GLY B 524  MET B 525  ARG B 528                    
SITE     3 AC8 11 HOH B1013  HOH B1050  HOH B1095                               
CRYST1   97.000  112.000  114.800  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010306  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008928  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008704        0.00000                         
MTRIX1   1 -0.843300  0.170100 -0.509800      128.05760    1                    
MTRIX2   1  0.104700  0.982400  0.154600      -62.61330    1                    
MTRIX3   1  0.527200  0.077000 -0.846300      -15.75990    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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